Human rhinovirus 2A proteinase cleavage sites in eukaryotic initiation factors (eIF) 4GI and eIF4GII are different

被引：23

作者：

Gradi, A

Svitkin, YV

Sommergruber, W

Imataka, H

Morino, S

Skern, T

Sonenberg, N

机构：

[1] McGill Univ, Dept Biochem, Montreal, PQ H3G 1Y6, Canada

[2] McGill Univ, McGill Canc Ctr, Montreal, PQ H3G 1Y6, Canada

[3] Boehringer Ingelheim GmbH & Co KG, Dept Exploratory Res, Vienna, Austria

[4] Univ Vienna, Vienna Bio Ctr, Div Biochem, Inst Med Biochem, Vienna, Austria

来源：

JOURNAL OF VIROLOGY | 2003年 / 77卷 / 08期

关键词：

D O I：

10.1128/JVI.77.8.5026-5029.2003

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

Several picornaviruses shut down host cellular protein synthesis by proteolytic cleavage of the eukaryotic initiation factor (eIF) 4GI and eIF4GII isoforms. Viral RNA translation is maintained by a cap-independent mechanism. Here, we identify the human rhinovirus 2 2A(pro) cleavage site in eIF4GII in vitro as PLLNV699*GSR; this sequence lies seven amino acids C-terminal to the cleavage site previously identified in eIF4GI (LSTR681*GPP).

引用

页码：5026 / 5029

页数：4

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